title: Disruption of rimP-SC, encoding a ribosome assembly cofactor, markedly enhances the production of several antibiotics in Streptomyces coelicolor.
abstract: BACKGROUND
  Ribosome assembly cofactor RimP is one of the auxiliary proteins required for maturation of the 30S subunit in Escherichia coli. Although RimP in protein synthesis is important, its role in secondary metabolites biosynthesis has not been reported so far. Considering the close relationship between protein synthesis and the production of secondary metabolites, the function of ribosome assembly cofactor RimP on antibiotics production was studied in Streptomyces coelicolor and Streptomyces venezuelae.
  
  
  RESULTS
  In this study, the rimP homologue rimP-SC was identified and cloned from Streptomyces coelicolor. Disruption of rimP-SC led to enhanced production of actinorhodin and calcium-dependent antibiotics by promoting the transcription of actII-ORF4 and cdaR. Further experiments demonstrated that MetK was one of the reasons for the increment of antibiotics production. In addition, rimP-SC disruption mutant could be used as a host to produce more peptidyl nucleoside antibiotics (polyoxin or nikkomycin) than the wild-type strain. Likewise, disruption of rimP-SV of Streptomyces venezuelae also significantly stimulated jadomycin production, suggesting that enhanced antibiotics production might be widespread in many other Streptomyces species.
  
  
  CONCLUSIONS
  These results established an important relationship between ribosome assembly cofactor and secondary metabolites biosynthesis and provided an approach for yield improvement of secondary metabolites in Streptomyces.
authors.affiliation: Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China.
authors.forename: Yuanyuan
authors.initials: Y
authors.lastname: Pan
authors.forename: Cheng
authors.initials: C
authors.lastname: Lu
authors.forename: Hailing
authors.initials: H
authors.lastname: Dong
authors.forename: Lingjun
authors.initials: L
authors.lastname: Yu
authors.forename: Gang
authors.initials: G
authors.lastname: Liu
authors.forename: Huarong
authors.initials: H
authors.lastname: Tan
mesh_terms: D000199:Actins / Q000235:genetics / Q000378:metabolism; D000595:Amino Acid Sequence; D000617:Aminoglycosides / Q000096:biosynthesis; D000880:Anthraquinones / Q000378:metabolism; D000900:Anti-Bacterial Agents / Q000096:biosynthesis*; D001426:Bacterial Proteins / Q000235:genetics* / Q000378:metabolism; D018533:Biomass; D050548:Catechol 1,2-Dioxygenase / Q000378:metabolism; D015801:Helminth Proteins / Q000235:genetics / Q000378:metabolism; D007546:Isoquinolines / Q000378:metabolism; D008716:Methionine Adenosyltransferase / Q000235:genetics / Q000378:metabolism; D008969:Molecular Sequence Data; D009285:Naphthoquinones / Q000378:metabolism; D011741:Pyrimidine Nucleosides / Q000096:biosynthesis; D054680:Ribosome Subunits, Small, Bacterial / Q000235:genetics* / Q000378:metabolism; D012270:Ribosomes / Q000378:metabolism; D016415:Sequence Alignment; D048372:Streptomyces coelicolor / Q000378:metabolism*; D014158:Transcription, Genetic; D000095622:Benzoisochromanequinones
chemical_list: D000199:Actins; D000617:Aminoglycosides; D000880:Anthraquinones; D000900:Anti-Bacterial Agents; D001426:Bacterial Proteins; D050548:Catechol 1,2-Dioxygenase; D015801:Helminth Proteins; D007546:Isoquinolines; D008716:Methionine Adenosyltransferase; D009285:Naphthoquinones; D011741:Pyrimidine Nucleosides; C431645:ACTII protein, Echinococcus granulosus; C506597:jadomycin A; C002457:polyoxin; C011952:nikkomycin; C013390:actinorhodin; D000095622:Benzoisochromanequinones